Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase

FEBS Letters

Volumn 582, Issue 28, 2008, Pages 3909-3914

  Teramoto, Takamasa ^a   Sakakibara, Yoichi ^b   Inada, Kanako ^c   Kurogi, Katsuhisa ^b   Liu, Ming Cheh ^d   Suiko, Masahito ^b   Kimura, Makoto ^a,c   Kakuta, Yoshimitsu ^a,c  

^a Department of Systems Life Sciences ^*  (Japan)

^b UNIVERSITY OF MIYAZAKI   (Japan)

^c KYUSHU UNIVERSITY   (Japan)

^d MEDICAL COLLEGE OF OHIO   (United States)

Author keywords

Catecholamine metabolism; Crystal structure; Substrate recognition; Sulfotransferase; SULT1D1

Indexed keywords

CATECHOLAMINE; SULFOTRANSFERASE; SULT1D1 SULFOTRANSFERASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; ENZYME BINDING; MOLECULAR MODEL; MOLECULAR RECOGNITION; MOUSE; MUTATION; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ALIGNMENT; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; ARYLSULFOTRANSFERASE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DNA MUTATIONAL ANALYSIS; DOPAMINE; HUMANS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SULFOTRANSFERASES;

MAMMALIA;

EID: 56049109501     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.10.035     Document Type: Article

References (24)

1. Coughtrie M.W., Sharp S., Maxwell K., and Innes N.P. Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases. Chem. Biol. Interact. 109 (1998) 3-27
2. Falany C.N. Enzymology of human cytosolic sulfotransferases. FASEB J. 11 (1997) 206-216
3. Sakakibara Y., Yanagisawa K., Takami Y., Nakayama T., Suiko M., and Liu M.C. Molecular cloning, expression, and functional characterization of novel mouse sulfotransferases. Biochem. Biophys. Res. Commun. 247 (1998) 681-686
4. Shimada M., Terazawa R., Kamiyama Y., Honma W., Nagata K., and Yamazoe Y. Unique properties of a renal sulfotransferase, St1d1, in dopamine metabolism. J. Pharmacol. Exp. Ther. 310 (2004) 808-814
5. Tsoi C., Falany C.N., Morgenstern R., and Swedmark S. Identification of a new subfamily of sulphotransferases: cloning and characterization of canine SULT1D1. Biochem. J. 356 (2001) 891-897
6. Tsoi C., Widersten M., Morgenstern R., and Swedmark S. Amino acid residue 247 in canine sulphotransferase SULT1D1: a new determinant of substrate selectivity. Biochem. J. 378 (2004) 687-692
7. Meinl W., and Glatt H. Structure and localization of the human SULT1B1 gene: neighborhood to SULT1E1 and a SULT1D pseudogene. Biochem. Biophys. Res. Commun. 288 (2001) 855-862
8. Lu J.H., Li H.T., Liu M.C., Zhang J.P., Li M., An X.M., and Chang W.R. Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3′-phosphoadenosine 5′-phosphate. Biochem. Biophys. Res. Commun. 335 (2005) 417-423
9. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
10. Vagin A., and Teplyakov A. An approach to multi-copy search in molecular replacement. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 1622-1624
11. Kakuta Y., Pedersen L.G., Carter C.W., Negishi M., and Pedersen L.C. Crystal structure of estrogen sulphotransferase. Nat. Struct. Biol. 4 (1997) 904-908
12. Morris R.J., Perrakis A., and Lamzin V.S. ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol. 374 (2003) 229-244
13. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 2126-2132
14. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53 (1997) 240-255
15. Vaguine A.A., Richelle J., and Wodak S.J. SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 191-205
16. Liu M.C., and Lipmann F. Decrease of tyrosine-O-sulfate-containing proteins found in rat fibroblasts infected with Rous sarcoma virus or Fujinami sarcoma virus. Proc. Natl. Acad. Sci. USA 81 (1984) 3695-3698
17. Kakuta Y., Petrotchenko E.V., Pedersen L.C., and Negishi M. The sulfuryl transfer mechanism. Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis. J. Biol. Chem. 273 (1998) 27325-32730
18. Gamage N.U., Duggleby R.G., Barnett A.C., Tresillian M., Latham C.F., Liyou N.E., McManus M.E., and Martin J.L. Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition. J. Biol. Chem. 278 (2003) 7655-7662
19. Dajani R., Hood A.M., and Coughtrie M.W. A single amino acid, glu146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3. Mol. Pharmacol. 54 (1998) 942-948
20. Brix L.A., Barnett A.C., Duggleby R.G., Leggett B., and McManus M.E. Analysis of the substrate specificity of human sulfotransferases SULT1A1 and SULT1A3: site-directed mutagenesis and kinetic studies. Biochemistry 38 (1999) 10474-10479
21. Brix L.A., Duggleby R.G., Gaedigk A., and McManus M.E. Structural characterization of human aryl sulphotransferases. Biochem. J. 337 Pt 2 (1999) 337-343
22. Chen G., Rabjohn P.A., York J.L., Wooldridge C., Zhang D., Falany C.N., and Radominska-Pandya A. Carboxyl residues in the active site of human phenol sulfotransferase (SULT1A1). Biochemistry 39 (2000) 16000-16007
23. Sakakibara Y., Takami Y., Nakayama T., Suiko M., and Liu M.C. Localization and functional analysis of the substrate specificity/catalytic domains of human M-form and P-form phenol sulfotransferases. J. Biol. Chem. 273 (1998) 6242-6247
24. Pai T.G., Oxendine I., Sugahara T., Suiko M., Sakakibara Y., and Liu M.C. Structure-function relationships in the stereospecific and manganese-dependent 3,4-dihydroxyphenylalanine/tyrosine-sulfating activity of human monoamine-form phenol sulfotransferase, SULT1A3. J. Biol. Chem. 278 (2003) 1525-1532